Differential Expression and Evolution of the Arabidopsis CYP86A Subfamily
Open Access
- 1 March 2005
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 137 (3) , 1067-1081
- https://doi.org/10.1104/pp.104.055715
Abstract
Some members of the Arabidopsis (Arabidopsis thaliana) CYP86A and CYP94B cytochrome P450 monooxygenase subfamilies, which share some sequence homology with the animal and fungal fatty acid hydroxylases, have been functionally defined as fatty acid ω-hydroxylases. With these activities, these and other fatty acid hydroxylases have potential roles in the synthesis of cutin, production of signaling molecules, and prevention of accumulation of toxic levels of free fatty acids. The constitutive and stress-inducible patterns of the five Arabidopsis CYP86A subfamily members have been defined in 7-d-old seedlings and 1-month-old plant tissues grown under normal conditions, and 7-d-old seedlings treated with different hormones (indole-3-acetic acid, abscisic acid, gibberellin, methyl jasmonic acid, brassinosteroid, salicylic acid), chemicals (clofibrate, 1-aminocyclopropane-1 carboxylic acid), or environmental stresses (cold, wounding, drought, mannitol, etiolation). Very distinct expression patterns exist for each of these fatty acid hydroxylases under normal growth conditions and in response to environmental and chemical stresses. Analysis of the promoter sequences for each of these genes with their expression patterns has highlighted a number of elements in current databases that potentially correlate with the responses of individual genes.Keywords
This publication has 52 references indexed in Scilit:
- Transgenic Arabidopsis Plants Expressing a Fungal Cutinase Show Alterations in the Structure and Properties of the Cuticle and Postgenital Organ FusionsPlant Cell, 2000
- Cucumber Hypocotyls Respond to Cutin Monomers via Both an Inducible and a Constitutive H2O2-Generating System1Plant Physiology, 1999
- Cloning and Functional Characterization of CYP94A2, a Medium Chain Fatty Acid Hydroxylase from Vicia sativaBiochemical and Biophysical Research Communications, 1999
- Cloning, Expression in Yeast, and Functional Characterization of CYP81B1, a Plant Cytochrome P450 That Catalyzes In-chain Hydroxylation of Fatty AcidsJournal of Biological Chemistry, 1998
- CYP86A1 fromArabidopsis thalianaEncodes a Cytochrome P450-Dependent Fatty Acid Omega-HydroxylaseBiochemical and Biophysical Research Communications, 1998
- The cytochrome P450 4 (CYP4) familyGeneral Pharmacology: The Vascular System, 1997
- Cytochrome P450-Dependent Oxidation of Fatty AcidsDrug Metabolism and Drug Interactions, 1995
- Diversity and Evolution of Plant P450 and P450-ReductasesDrug Metabolism and Drug Interactions, 1995
- CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choiceNucleic Acids Research, 1994
- Hydroxy and normal fatty acid distribution in stigmas of Nicotiana and other plantsPhytochemistry, 1988